Small-molecule perturbation of competing interactions between c-Myc and Max

Intrinsically unstructured proteins and their functions

Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871 · see citing works

Towards a proteome-scale map of the human protein–protein interaction network

Rual, J.-F. M., Venkatesan, K., Hao, T., Hirozane-Kishikawa, T., Dricot, A., Li, N., Berriz, G. F., Gibbons, F. D., Dreze, M., Ayivi-Guedehoussou, N., et al. (2005) · Nature · doi:10.1038/nature04209 · Cited by 2,904 · see citing works

Evidence for dynamically organized modularity in the yeast protein–protein interaction network

Han, J. J., Bertin, N., Hao, T., Goldberg, D. S., Berriz, G. F., Zhang, L. V., Dupuy, D., Walhout, A. J. M., Cusick, M. E., Roth, F. P., et al. (2004) · Nature · doi:10.1038/nature02555 · Cited by 1,789 · see citing works

c-Myc Target Genes Involved in Cell Growth, Apoptosis, and Metabolism

Dang, C. V. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.1 · Cited by 1,707 · see citing works

Transcription factors: structural families and principles of DNA recognition.

Pabo, C., & Sauer, R. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.005201 · Cited by 1,445 · see citing works

Coupling of folding and binding for unstructured proteins

Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327 · see citing works

Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins

Iakoucheva, L. M., Brown, C. J., Lawson, J. D., Obradović, Z., & Dunker, A. K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00969-5 · Cited by 1,214 · see citing works

Navigating chemical space for biology and medicine

Lipinski, C. A., & Hopkins, A. L. (2004) · Nature · doi:10.1038/nature03193 · Cited by 1,008 · see citing works

Modular organization of cellular networks

Rives, A. W., & Galitski, T. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0237338100 · Cited by 695 · see citing works

X-Ray Structures of Myc-Max and Mad-Max Recognizing DNA

Nair, S. K., & Burley, S. K. (2003) · Cell · doi:10.1016/s0092-8674(02)01284-9 · Cited by 551 · see citing works

Structural disorder throws new light on moonlighting

Tompa, P., Szász, C., & Buday, L. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.07.008 · Cited by 468 · see citing works

Comprehensive Identification of Human bZIP Interactions with Coiled-Coil Arrays

Newman, J. R. S., & Keating, A. E. (2003) · Science · doi:10.1126/science.1084648 · Cited by 449 · see citing works

Low molecular weight inhibitors of Myc–Max interaction and function

Yin, X., Giap, C., Lazo, J. S., & Prochownik, E. V. (2003) · Oncogene · doi:10.1038/sj.onc.1206641 · Cited by 426 · see citing works

Small-molecule antagonists of Myc/Max dimerization inhibit Myc-induced transformation of chicken embryo fibroblasts

Berg, T., Cohen, S. B., Desharnais, J., Sonderegger, C. K., Maslyar, D. J., Goldberg, J., Boger, D. L., & Vogt, P. K. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.062036999 · Cited by 326 · see citing works

Helix-loop-helix proteins as regulators of muscle-specific transcription.

Edmondson, D. G., & Olson, E. N. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53995-8 · Cited by 273 · see citing works

Improved low molecular weight Myc-Max inhibitors

Wang, H., Hammoudeh, D. I., Follis, A. V., Reese, B. E., Lazo, J. S., Metallo, S. J., & Prochownik, E. V. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-0005 · Cited by 191 · see citing works

The crystal structure of an intact human Max–DNA complex: new insights into mechanisms of transcriptional control

Brownlie, P. D., Ceska, T. A., Lamers, M. H., Romier, C., Stier, G., Teo, H., & Suck, D. (1997) · Structure · doi:10.1016/s0969-2126(97)00207-4 · Cited by 169 · see citing works

Visualization of Myc/Max/Mad Family Dimers and the Competition for Dimerization in Living Cells

Grinberg, A. V., Hu, C., & Kerppola, T. K. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4294-4308.2004 · Cited by 169 · see citing works

Cancer therapeutics: Targeting the dark side of Myc

Ponzielli, R., Katz, S., Baršytė-Lovejoy, D., & Penn, L. Z. (2005) · European Journal of Cancer · doi:10.1016/j.ejca.2005.08.017 · Cited by 166 · see citing works

Natively Disordered Proteins

Romero, P. R., Zoran Obradovic, A., & Dunker, A. K. (2004) · Applied Bioinformatics · doi:10.2165/00822942-200403020-00005 · Cited by 163 · see citing works

Selective Inhibition of c-Myc/Max Dimerization and DNA Binding by Small Molecules

Kiessling, A., Sperl, B., Hollis, A., Eick, D., & Berg, T. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.05.011 · Cited by 148 · see citing works

Myc and Max function as a nucleoprotein complex

Blackwood, E. M., Kretzner, L., & Eisenman, R. N. (1992) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(05)80278-3 · Cited by 141 · see citing works

Transcriptional Repression in Eukaryotes

Herschbach, B. M., & Johnson, A. D. (1993) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.09.110193.002403 · Cited by 116 · see citing works

A credit-card library approach for disrupting protein–protein interactions

Xu, Y., Shi, J., Yamamoto, N., Moss, J. A., Vogt, P. K., & Janda, K. D. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.11.052 · Cited by 93 · see citing works

Identification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers.

Bousset, K., Henriksson, M., Lüscher‐Firzlaff, J., Litchfield, D. W., & Lüscher, B. (1993) · PubMed · Cited by 79 · see citing works

Differential patterns of DNA binding by myc and max proteins.

Prochownik, E., & VanAntwerp, M. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.3.960 · Cited by 69 · see citing works

Assembly of b/HLH/z Proteins c-Myc, Max, and Mad1 with Cognate DNA: Importance of Protein−Protein and Protein−DNA Interactions

Hu, J., Banerjee, A., & Goss, D. J. (2005) · Biochemistry · doi:10.1021/bi050206i · Cited by 49 · see citing works

Distinct Roles for MAX Protein Isoforms in Proliferation and Apoptosis

Zhang, H., Fan, S., & Prochownik, E. V. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.28.17416 · Cited by 48 · see citing works

MYC on the Path to Cancer

Dang, C. V. (2012) · Cell · doi:10.1016/j.cell.2012.03.003 · Cited by 3,390 · see citing works

Understanding protein non-folding

Uversky, V. N., & Dunker, A. K. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.01.017 · Cited by 1,188 · see citing works

Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases

Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288 · see citing works

Small Molecules Targeting c-Myc Oncogene: Promising Anti-Cancer Therapeutics

Chen, B.-J., Wu, Y., Tanaka, Y., & Zhang, W. (2014) · International Journal of Biological Sciences · doi:10.7150/ijbs.10190 · Cited by 247 · see citing works

Emerging Roles of C-Myc in Cancer Stem Cell-Related Signaling and Resistance to Cancer Chemotherapy: A Potential Therapeutic Target Against Colorectal Cancer

Elbadawy, M., Usui, T., Yamawaki, H., & Sasaki, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092340 · Cited by 237 · see citing works

A complex task? Direct modulation of transcription factors with small molecules

Koehler, A. N. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.03.022 · Cited by 189 · see citing works

Ablation of Fbxw7 Eliminates Leukemia-Initiating Cells by Preventing Quiescence

Takeishi, S., Matsumoto, A., Onoyama, I., Naka, K., Hirao, A., & Nakayama, K. I. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.01.026 · Cited by 177 · see citing works

Expanding the proteome: disordered and alternatively folded proteins

Dyson, H. J. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583511000060 · Cited by 173 · see citing works

Small-molecule inhibitors of the Myc oncoprotein

Fletcher, S., & Prochownik, E. V. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.005 · Cited by 153 · see citing works

Synthetic Lethality of PARP Inhibitors in Combination with MYC Blockade Is Independent of BRCA Status in Triple-Negative Breast Cancer

Carey, J. P. W., Karakaş, C., Bui, T. N., Chen, X., Vijayaraghavan, S., Zhao, Y., Wang, J., Mikule, K. W., Litton, J. K., Hunt, K. K., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-1494 · Cited by 145 · see citing works

Mission Possible: Advances in MYC Therapeutic Targeting in Cancer

Allen-Petersen, B. L., & Sears, R. C. (2019) · BioDrugs · doi:10.1007/s40259-019-00370-5 · Cited by 143 · see citing works

Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D2concept

Uversky, V. N. (2010) · Expert Review of Proteomics · doi:10.1586/epr.10.36 · Cited by 141 · see citing works

In Vitro Cytotoxicity and In Vivo Efficacy, Pharmacokinetics, and Metabolism of 10074-G5, a Novel Small-Molecule Inhibitor of c-Myc/Max Dimerization

Clausen, D. M., Guo, J., Parise, R. A., Beumer, J. H., Egorin, M. J., Lazo, J. S., Prochownik, E. V., & Eiseman, J. L. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.170555 · Cited by 117 · see citing works

Intrinsically disordered proteins and biomolecular condensates as drug targets

Biesaga, M., Frigolé-Vivas, M., & Salvatella, X. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.02.009 · Cited by 115 · see citing works

Homologous Recombination Deficiency in Ovarian, Breast, Colorectal, Pancreatic, Non-Small Cell Lung and Prostate Cancers, and the Mechanisms of Resistance to PARP Inhibitors

Mekonnen, N., Yang, H., & Shin, Y. K. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.880643 · Cited by 113 · see citing works

Targeting intrinsically disordered proteins involved in cancer

Santofimia‐Castaño, P., Rizzuti, B., Xia, Y., Abián, O., Peng, L., Velázquez‐Campoy, A., Neira, J. L., & Iovanna, J. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03347-3 · Cited by 110 · see citing works

Structural and Biophysical Insights into the Function of the Intrinsically Disordered Myc Oncoprotein

Beaulieu, M.-È., Castillo, F., & Soucek, L. (2020) · Cells · doi:10.3390/cells9041038 · Cited by 110 · see citing works

Strategically targeting MYC in cancer

Posternak, V., & Cole, M. D. (2016) · F1000Research · doi:10.12688/f1000research.7879.1 · Cited by 107 · see citing works

Targeting disordered proteins with small molecules using entropy

Heller, G. T., Sormanni, P., & Vendruscolo, M. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.07.004 · Cited by 104 · see citing works

Targeting of the MYCN Protein with Small Molecule c-MYC Inhibitors

Müller, I., Larsson, K., Frenzel, A., Oliynyk, G., Zirath, H., Prochownik, E. V., Westwood, N. J., & Arsenian‐Henriksson, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0097285 · Cited by 96 · see citing works

Inhibition of c-Myc Overcomes Cytotoxic Drug Resistance in Acute Myeloid Leukemia Cells by Promoting Differentiation

Pan, X.-N., Chen, J.-J., Wang, L.-X., Xiao, R.-Z., Liu, L.-L., Fang, Z.-G., Liu, Q., Long, Z., & Lin, D.-J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105381 · Cited by 82 · see citing works

The Impact of Small Molecule Binding on the Energy Landscape of the Intrinsically Disordered Protein C-Myc

Michel, J., & Cuchillo, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041070 · Cited by 74 · see citing works

Sequence Specificity in the Entropy-Driven Binding of a Small Molecule and a Disordered Peptide

Heller, G. T., Aprile, F. A., Bonomi, M., Camilloni, C., Simone, A. D., & Vendruscolo, M. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.07.016 · Cited by 64 · see citing works

Methods of probing the interactions between small molecules and disordered proteins

Heller, G. T., Aprile, F. A., & Vendruscolo, M. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2563-4 · Cited by 62 · see citing works

Disruption of Myc-Max Heterodimerization with Improved Cell-Penetrating Analogs of the Small Molecule 10074-G5

Wang, H., Chauhan, J., Hu, A., Pendleton, K. P., Yap, J. L., Sabato, P. E., Jones, J. W., Perri, M., Yu, J., Cione, E., et al. (2013) · Oncotarget · doi:10.18632/oncotarget.1108 · Cited by 57 · see citing works

Prion-Like Proteins in Phase Separation and Their Link to Disease

Sprunger, M. L., & Jackrel, M. E. (2021) · Biomolecules · doi:10.3390/biom11071014 · Cited by 57 · see citing works

Intravesical Instillation of c-MYC Inhibitor KSI-3716 Suppresses Orthotopic Bladder Tumor Growth

Jeong, K., Kim, K., Seo, H.-H., Shin, S.-P., Ahn, K.-O., Ji, M.-J., Park, W. S., Kim, I.-H., Lee, S.-J., & Seo, H. K. (2013) · The Journal of Urology · doi:10.1016/j.juro.2013.07.019 · Cited by 55 · see citing works

Blimp1+ cells generate functional mouse sebaceous gland organoids in vitro

Feldman, A., Mukha, D., Maor, I. I., Sedov, E., Koren, E., Yosefzon, Y., Shlomi, T., & Fuchs, Y. (2019) · Nature Communications · doi:10.1038/s41467-019-10261-6 · Cited by 52 · see citing works

Structurally diverse c-Myc inhibitors share a common mechanism of action involving ATP depletion

Wang, H., Sharma, L., Lu, J. L., Finch, P., Fletcher, S., & Prochownik, E. V. (2015) · Oncotarget · doi:10.18632/oncotarget.4327 · Cited by 41 · see citing works

Inhibiting MYC binding to the E-box DNA motif by ME47 decreases tumour xenograft growth

Lustig, L. C., Dingar, D. D., Tu, W. B., Lourenco, C., Kalkat, M., Inamoto, I., Ponzielli, R., Chan, W. C. W., Shin, J. A., & Penn, L. Z. (2017) · Oncogene · doi:10.1038/onc.2017.275 · Cited by 41 · see citing works

Protein homodimer sequestration with small molecules: Focus on PD-L1

Bailly, C., & Vergoten, G. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113821 · Cited by 38 · see citing works

MYC the oncogene from hell: Novel opportunities for cancer therapy

Papadimitropoulou, A., Makri, M., & Zoidis, G. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116194 · Cited by 38 · see citing works

Targeting protein–protein interactions (PPIs) of transcription factors: Challenges of intrinsically disordered proteins (IDPs) and regions (IDRs)

Sammak, S., & Zinzalla, G. (2015) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2015.06.004 · Cited by 37 · see citing works

Mechanisms of small-molecule binding to intrinsically disordered proteins

Cuchillo, R., & Michel, J. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120086 · Cited by 36 · see citing works

Role of TGF-β signaling in uterine carcinosarcoma

Dwivedi, S. K. D., McMeekin, S., Slaughter, K. N., & Bhattacharya, R. (2015) · Oncotarget · doi:10.18632/oncotarget.3711 · Cited by 27 · see citing works

Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration

Panova, S., Cliff, M. J., Macek, P., Blackledge, M. J., Jensen, M. R., Nissink, J. W. M., Embrey, K. J., Davies, R., & Waltho, J. P. (2019) · Structure · doi:10.1016/j.str.2019.07.006 · Cited by 23 · see citing works

c-Myc promotes cholangiocarcinoma cells to overcome contact inhibition via the mTOR pathway

Luo, G., Li, B., Duan, C., Cheng, Y., Xiao, B., Yao, F., Wei, M., Tao, Q., Feng, C., Xia, X., et al. (2017) · Oncology Reports · doi:10.3892/or.2017.5913 · Cited by 22 · see citing works

A quantitative, surface plasmon resonance-based approach to evaluating DNA binding by the c-Myc oncoprotein and its disruption by small molecule inhibitors

Wang, H., Ramakrishnan, A., Fletcher, S., & Prochownik, E. V. (2015) · Journal of Biological Methods · doi:10.14440/jbm.2015.54 · Cited by 20 · see citing works

Reverse Engineering the Neuroblastoma Regulatory Network Uncovers MAX as One of the Master Regulators of Tumor Progression

Albanus, R. D., Dalmolin, R. J. S., Castro, M. A. A., Pasquali, M. A. D. B., Ramos, V. D. M., Gelain, D. P., & Moreira, J. C. F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082457 · Cited by 14 · see citing works

Lipid Metabolic Reprogramming in Embryonal Neoplasms with MYCN Amplification

Talapatra, J., & Reddy, M. M. (2023) · Cancers · doi:10.3390/cancers15072144 · Cited by 12 · see citing works

Multistage modeling of protein dynamics with monomeric Myc oncoprotein as an example

Liu, J., Dai, J., He, J., Niemi, A. J., & Ilieva, N. (2017) · Physical review. E · doi:10.1103/physreve.95.032406 · Cited by 8 · see citing works

Computational Strategies in Cancer Drug Discovery

Mustata, G. I., & Muftuoglu, Y. (2012) · InTech eBooks · doi:10.5772/24177 · Cited by 7 · see citing works

High-throughput structure determination of an intrinsically disordered protein using cell-free protein crystallization

Kojima, M., Abe, S., Furuta, T., Hirata, K., Yao, X., Kobayashi, A., Kobayashi, R., & Ueno, T. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2322452121 · Cited by 6 · see citing works

Innovative approaches in skin therapy: The rise of organoid cultivation

Zhou, R., Luo, X., Chen, S., Jia, K., Yu, H., Huang, Z., Tan, Y., Ma, M., Zhao, J., Xing, J., et al. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.162248 · Cited by 6 · see citing works

cAMP-Dependent Protein Kinase A (PKA)–Mediated c-Myc Degradation Is Dependent on the Relative Proportion of PKA-I and PKA-II Isozymes

Liu, Q., Nguyen, É., Døskeland, S. O., & Ségal-Bendirdjian, É. (2015) · Molecular Pharmacology · doi:10.1124/mol.115.097915 · Cited by 6 · see citing works

Molecular cloning and functional characterization of MYC transcription factor in pathogen-challenged Apostichopus japonicus

Zhang, Y., Shao, Y., Lv, Z., Zhang, W., Zhao, X., Guo, M. Z., & Li, C. (2019) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2019.103487 · Cited by 6 · see citing works

MYC and MXI1 Protein Expression: Potential Prognostic Significance in Women with Breast Cancer in China

Xu, L., Sun, Y., Li, W., Mai, L., Guo, Y., & Fan, Q.-X. (2014) · Oncology Research and Treatment · doi:10.1159/000360207 · Cited by 5 · see citing works

S146L in MYC is a context-dependent activating substitution in cancer development

Hinds, J. W., Feris, E. J., Wilkins, O. M., Deary, L. T., Wang, X., & Cole, M. D. (2022) · PLoS ONE · doi:10.1371/journal.pone.0272771 · Cited by 4 · see citing works

Targeting an Interaction Between Two Disordered Domains by Using a Designed Peptide

Mayer, G., Shpilt, Z., Bressler, S., Marcu, O., Schueler‐Furman, O., Tshuva, E. Y., & Friedler, A. (2020) · Chemistry - A European Journal · doi:10.1002/chem.202000465 · Cited by 4 · see citing works

A Hybrid G-Quadruplex Structure Formed by a Sequence from the MAX Gene

Hu, X., Xiao, N., Lan, W., & Cao, C. (2025) · JACS Au · doi:10.1021/jacsau.5c01247 · Cited by 3 · see citing works

Morphological inhibitors of aggregation-prone amyloid- β conformers: A computational exploration

Bosio, S., Falchi, F., Rauzi, C., & Bellucci, L. (2025) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2025.110545 · Cited by 2 · see citing works

A Hybrid compound H93 treats prostate cancer by directly binding UHRF1 and promoting protein dimerization

Fu, Y., Jiang, L., Xie, G., Peng, Y., Fu, Y., Zhu, Q., Liu, Y., Zhao, G., Liu, X., Peng, Y., et al. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01744-3 · Cited by 2 · see citing works

Probing the Structural Dynamics of the Unbound MAX Protein: Insights from Well-Tempered Metadynamics

Lu, H., Marti, J., & Faraudo, J. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c02155 · Cited by 1 · see citing works

The Notch1-c-Myc Pathway Mediates Leukemia-Initiating Cell Activity in Mouse T-ALL Models: A Dissertation

Tesell, J. (2013) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/m2nc8v

Targeting MYC and Exploring the Role of Mitochondrial Metabolism in Childhood Neuroblastoma

Zirath, H. (2014) · Figshare

Bringing order to disorder : structural and functional analysis for development of strategies to target myc

Müller, I. (2014) · Figshare

Inhibition of castration resistant prostate cancer by sintokamide A : an antagonist of the amino-terminus of the androgen receptor

Tavakoli, I. (2013) · cIRcle (University of British Columbia) · doi:10.14288/1.0072850

The Functions and Regulatory Chemicals of Human Leucine Zipper Transcription Factors (LZ TFs)

Yang, H., Bi, S., Yu, B., Fang, P., & Wang, J. (2025) · 化学学报 · doi:10.6023/a25020042

BindingDB Entry 50021153: MYC the oncogene from hell: Novel opportunities for cancer therapy.

BindingDB (2025) · UC San Diego · doi:10.7270/q2qz2gkz

Potent Inhibitors Of c-Myc-Max Dimerization Through Multivalent Binding To The Intrinsically Disordered c-Myc Monomer

Follis, A. V., Hammoudeh, D. I., Wang, H., Prochownik, E. V., & Metallo, S. J. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.12.2273

Small-molecule Inhibitors of Myc–Max Interaction and DNA Binding

Fletcher, S., & Prochownik, E. V. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016544-00302

The Max homodimeric b‐HLH‐LZ significantly interferes with the specific heterodimerization between the c‐Myc and Max b‐HLH‐LZ in absence of DNA: a quantitative analysis

McDuff, F., Naud, J., Montagne, M., Sauvé, S., & Lavigne, P. (2009) · Journal of Molecular Recognition · doi:10.1002/jmr.938 · Cited by 26 · see citing works

Structural Rationale for the Coupled Binding and Unfolding of the c-Myc Oncoprotein by Small Molecules

Follis, A. V., Hammoudeh, D. I., Wang, H., Prochownik, E. V., & Metallo, S. J. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.09.011 · Cited by 183 · see citing works

Alanine Scan of a Small Molecule Interaction Site on the Disordered c-Myc Oncoprotein

Fred, L. M., Zablotsky, B. L., Gerhart, K. P., & Metallo, S. J. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2010.12.532